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Protein

Chemotaxis response regulator protein-glutamate methylesterase

Gene

cheB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR.

Catalytic activityi

Protein L-glutamate O5-methyl ester + H2O = protein L-glutamate + methanol.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei164By similarity1
Active sitei190By similarity1
Active sitei286By similarity1

GO - Molecular functioni

  • deaminase binding Source: CAFA
  • phosphorelay response regulator activity Source: InterPro
  • protein-glutamate methylesterase activity Source: CAFA

GO - Biological processi

  • chemotaxis Source: EcoliWiki
  • protein deamination Source: CAFA
  • protein demethylation Source: CAFA

Keywordsi

Molecular functionHydrolase
Biological processChemotaxis

Enzyme and pathway databases

BioCyciEcoCyc:CHEB-MONOMER.
MetaCyc:CHEB-MONOMER.
BRENDAi3.1.1.61. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Chemotaxis response regulator protein-glutamate methylesterase (EC:3.1.1.61)
Gene namesi
Name:cheB
Ordered Locus Names:b1883, JW1872
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10147. cheB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • plasma membrane Source: CAFA

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001579921 – 349Chemotaxis response regulator protein-glutamate methylesteraseAdd BLAST349

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei564-aspartylphosphateBy similarity1

Post-translational modificationi

Phosphorylated by CheA. Phosphorylation suppresses the inhibitory activity of the N-terminal domain.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP07330.
PRIDEiP07330.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
cheAP073633EBI-1125895,EBI-1026773

GO - Molecular functioni

  • deaminase binding Source: CAFA

Protein-protein interaction databases

BioGridi4260716. 220 interactors.
DIPiDIP-9272N.
IntActiP07330. 10 interactors.
STRINGi316385.ECDH10B_2024.

Structurei

3D structure databases

ProteinModelPortaliP07330.
SMRiP07330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 122Response regulatoryPROSITE-ProRule annotationAdd BLAST118
Domaini152 – 344CheB-type methylesteraseAdd BLAST193

Domaini

The N-terminal regulatory domain inhibits the activity of the C-terminal effector domain.

Phylogenomic databases

eggNOGiENOG4105CMP. Bacteria.
COG2201. LUCA.
HOGENOMiHOG000151423.
InParanoidiP07330.
KOiK03412.
PhylomeDBiP07330.

Family and domain databases

CDDicd16432. CheB_Rec. 1 hit.
cd00156. REC. 1 hit.
Gene3Di3.40.50.180. 1 hit.
HAMAPiMF_00099. CheB_methylest. 1 hit.
InterProiView protein in InterPro
IPR035909. CheB_C.
IPR011006. CheY-like_superfamily.
IPR008248. Sig_transdc_resp-reg_CheB.
IPR000673. Sig_transdc_resp-reg_Me-estase.
IPR001789. Sig_transdc_resp-reg_receiver.
PfamiView protein in Pfam
PF01339. CheB_methylest. 1 hit.
PF00072. Response_reg. 1 hit.
PIRSFiPIRSF000876. RR_chemtxs_CheB. 1 hit.
SMARTiView protein in SMART
SM00448. REC. 1 hit.
SUPFAMiSSF52172. SSF52172. 1 hit.
SSF52738. SSF52738. 1 hit.
PROSITEiView protein in PROSITE
PS50122. CHEB. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.

Sequencei

Sequence statusi: Complete.

P07330-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKIRVLSVD DSALMRQIMT EIINSHSDME MVATAPDPLV ARDLIKKFNP
60 70 80 90 100
DVLTLDVEMP RMDGLDFLEK LMRLRPMPVV MVSSLTGKGS EVTLRALELG
110 120 130 140 150
AIDFVTKPQL GIREGMLAYN EMIAEKVRTA AKASLAAHKP LSAPTTLKAG
160 170 180 190 200
PLLSSEKLIA IGASTGGTEA IRHVLQPLPL SSPALLITQH MPPGFTRSFA
210 220 230 240 250
DRLNKLCQIG VKEAEDGERV LPGHAYIAPG DRHMELSRSG ANYQIKIHDG
260 270 280 290 300
PAVNRHRPSV DVLFHSVAKQ AGRNAVGVIL TGMGNDGAAG MLAMRQAGAW
310 320 330 340
TLAQNEASCV VFGMPREAIN MGGVCEVVDL SQVSQQMLAK ISAGQAIRI
Length:349
Mass (Da):37,468
Last modified:November 1, 1997 - v3
Checksum:i6F3D1AFB8D23D3F5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti96A → P in AAA23569 (PubMed:3510184).Curated1
Sequence conflicti125E → Q in AAA23569 (PubMed:3510184).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13463 Genomic DNA. Translation: AAA23569.1.
U00096 Genomic DNA. Translation: AAC74953.1.
AP009048 Genomic DNA. Translation: BAA15699.1.
PIRiD25195. XYECEB.
RefSeqiNP_416397.1. NC_000913.3.
WP_000036361.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74953; AAC74953; b1883.
BAA15699; BAA15699; BAA15699.
GeneIDi946394.
KEGGiecj:JW1872.
eco:b1883.
PATRICifig|1411691.4.peg.364.

Similar proteinsi

Entry informationi

Entry nameiCHEB_ECOLI
AccessioniPrimary (citable) accession number: P07330
Secondary accession number(s): P78070
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: November 22, 2017
This is version 152 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene